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Protein Page:
HBA1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
HBA1 Involved in oxygen transport from the lung to the various peripheral tissues. Defects in HBA1 may be a cause of Heinz body anemias (HEIBAN). This is a form of non-spherocytic hemolytic anemia of Dacie type 1. After splenectomy, which has little benefit, basophilic inclusions called Heinz bodies are demonstrable in the erythrocytes. Before splenectomy, diffuse or punctate basophilia may be evident. Most of these cases are probably instances of hemoglobinopathy. The hemoglobin demonstrates heat lability. Heinz bodies are observed also with the Ivemark syndrome (asplenia with cardiovascular anomalies) and with glutathione peroxidase deficiency. Defects in HBA1 are the cause of alpha-thalassemia (A- THAL). The thalassemias are the most common monogenic diseases and occur mostly in Mediterranean and Southeast Asian populations. The hallmark of alpha-thalassemia is an imbalance in globin-chain production in the adult HbA molecule. The level of alpha chain production can range from none to very nearly normal levels. Deletion of both copies of each of the two alpha-globin genes causes alpha(0)-thalassemia, also known as homozygous alpha thalassemia. Due to the complete absence of alpha chains, the predominant fetal hemoglobin is a tetramer of gamma-chains (Bart hemoglobin) that has essentially no oxygen carrying capacity. This causes oxygen starvation in the fetal tissues leading to prenatal lethality or early neonatal death. The loss of three alpha genes results in high levels of a tetramer of four beta chains (hemoglobin H), causing a severe and life-threatening anemia known as hemoglobin H disease. Untreated, most patients die in childhood or early adolescence. The loss of two alpha genes results in mild alpha-thalassemia, also known as heterozygous alpha-thalassemia. Affected individuals have small red cells and a mild anemia (microcytosis). If three of the four alpha-globin genes are functional, individuals are completely asymptomatic. Some rare forms of alpha-thalassemia are due to point mutations (non- deletional alpha-thalassemia). The thalassemic phenotype is due to unstable globin alpha chains that are rapidly catabolized prior to formation of the alpha-beta heterotetramers. Alpha(0)-thalassemia is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non- immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end-stage of a wide variety of disorders. Defects in HBA1 are the cause of hemoglobin H disease (HBH). HBH is a form of alpha-thalassemia due to the loss of three alpha genes. This results in high levels of a tetramer of four beta chains (hemoglobin H), causing a severe and life-threatening anemia. Untreated, most patients die in childhood or early adolescence. Belongs to the globin family. Note: This description may include information from UniProtKB.
Protein type: Carrier protein
Chromosomal Location of Human Ortholog: 16p13.3
Reference #:  P69905 (UniProtKB)
Alt. Names/Synonyms: alpha one globin; alpha-1 globin; alpha-1-globin; Alpha-globin; CD31; HBA; HBA1; HBA2; hemoglobin alpha 1 globin chain; Hemoglobin alpha chain; hemoglobin alpha-1 chain; Hemoglobin subunit alpha; hemoglobin, alpha 1; MGC126895; MGC126897
Gene Symbols: HBA1, HBA2
Molecular weight: 15,258 Da
Basal Isoelectric point: 8.72  Predict pI for various phosphorylation states
Select Structure to View Below

HBA1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 7 S4-p ____MVLsPADktNV
0 1 S4-gl ____MVLsPADktNV
0 4 K8-ac MVLsPADktNVkAAW
0 13 K8 MVLsPADKtNVkAAW
0 7 T9-p VLsPADktNVkAAWG
0 10 K12-ac PADktNVkAAWGkVG
0 13 K12 PADktNVKAAWGkVG
0 10 K17-ac NVkAAWGkVGAHAGE
0 7 K17-ub NVkAAWGkVGAHAGE
0 1298 Y25-p VGAHAGEyGAEALER
0 9 S36-p ALERMFLsFPTtkty
0 1 S36-gl ALERMFLsFPTtkty
0 1 T40-p MFLsFPTtktyFPHF
0 19 K41-ac FLsFPTtktyFPHFD
0 18 K41-ub FLsFPTtktyFPHFD
0 10 T42-p LsFPTtktyFPHFDL
0 79 Y43-p sFPTtktyFPHFDLs
0 5 S50-p yFPHFDLsHGsAQVk
0 5 S53-p HFDLsHGsAQVkGHG
0 16 K57-ac sHGsAQVkGHGkkVA
0 11 K57-ub sHGsAQVkGHGkkVA
0 6 K61-ac AQVkGHGkkVADALT
0 1 K61-ub AQVkGHGkkVADALT
0 1 K62-ac QVkGHGkkVADALTN
0 2 K62 QVkGHGkKVADALTN
0 1 K62 QVkGHGkKVADALTN
0 14 K91-ac LSDLHAHkLRVDPVN
0 16 K91 LSDLHAHKLRVDPVN
0 28 K100-ac RVDPVNFkLLSHCLL
0 1 K100 RVDPVNFKLLSHCLL
0 2 S103 PVNFkLLSHCLLVtL
0 3 T109-p LSHCLLVtLAAHLPA
0 2 A112 CLLVtLAAHLPAEFT
0 1 S125 FTPAVHASLDKFLAS
0 12 S132 SLDKFLASVsTVLTs
0 1 S134-gl DKFLASVsTVLTsky
0 7 T135 KFLASVsTVLTskyR
0 3 T138 ASVsTVLTskyR___
0 2 S139-p SVsTVLTskyR____
0 4 K140-ac VsTVLTskyR_____
0 2 K140 VsTVLTsKyR_____
0 9 Y141-p sTVLTskyR______
  mouse

 
S4-p ____MVLsGEDksNI
S4 ____MVLSGEDksNI
K8-ac MVLsGEDksNIkAAW
K8-ub MVLsGEDksNIkAAW
S9-p VLsGEDksNIkAAWG
K12 GEDksNIKAAWGkIG
K12-ub GEDksNIkAAWGkIG
K17-ac NIkAAWGkIGGHGAE
K17-ub NIkAAWGkIGGHGAE
Y25-p IGGHGAEyGAEALER
S36-p ALERMFAsFPTtkTy
S36 ALERMFASFPTtkTy
T40-p MFAsFPTtkTyFPHF
K41-ac FAsFPTtkTyFPHFD
K41-ub FAsFPTtkTyFPHFD
T42 AsFPTtkTyFPHFDV
Y43-p sFPTtkTyFPHFDVs
S50-p yFPHFDVsHGsAQVk
S53-p HFDVsHGsAQVkGHG
K57-ac sHGsAQVkGHGkkVA
K57-ub sHGsAQVkGHGkkVA
K61-ac AQVkGHGkkVADALA
K61 AQVkGHGKkVADALA
K62 QVkGHGkKVADALAS
K62-m1 QVkGHGkkVADALAS
K62-ub QVkGHGkkVADALAS
K91-ac LSDLHAHkLRVDPVN
K91-ub LSDLHAHkLRVDPVN
K100-ac RVDPVNFkLLsHCLL
K100-ub RVDPVNFkLLsHCLL
S103-p PVNFkLLsHCLLVtL
T109-p LsHCLLVtLAsHHPA
S112-p CLLVtLAsHHPADFT
S125-p FTPAVHAsLDKFLAs
S132-p sLDKFLAsVStVLts
S134 DKFLAsVStVLtskY
T135-p KFLAsVStVLtskYR
T138-p AsVStVLtskYR___
S139-p sVStVLtskYR____
K140-ac VStVLtskYR_____
K140-ub VStVLtskYR_____
Y141 StVLtskYR______
  rat

 
S4-p ____MVLsADDKTNI
S4 ____MVLSADDKTNI
K8 MVLsADDKTNIkNCW
K8 MVLsADDKTNIkNCW
T9 VLsADDKTNIkNCWG
K12-ac ADDKTNIkNCWGkIG
K12-ub ADDKTNIkNCWGkIG
K17-ac NIkNCWGkIGGHGGE
K17 NIkNCWGKIGGHGGE
Y25-p IGGHGGEyGEEALQR
A36 ALQRMFAAFPTTkTY
A36 ALQRMFAAFPTTkTY
T40 MFAAFPTTkTYFSHI
K41-ac FAAFPTTkTYFSHID
K41-ub FAAFPTTkTYFSHID
T42 AAFPTTkTYFSHIDV
Y43 AFPTTkTYFSHIDVs
S50-p YFSHIDVsPGSAQVk
S53 HIDVsPGSAQVkAHG
K57-ac sPGSAQVkAHGkkVA
K57-ub sPGSAQVkAHGkkVA
K61-ac AQVkAHGkkVADALA
K61 AQVkAHGKkVADALA
K62-ac QVkAHGkkVADALAK
K62 QVkAHGkKVADALAK
K62 QVkAHGkKVADALAK
K91-ac LSDLHAHkLRVDPVN
K91-ub LSDLHAHkLRVDPVN
K100 RVDPVNFKFLSHCLL
K100 RVDPVNFKFLSHCLL
S103 PVNFKFLSHCLLVTL
T109 LSHCLLVTLACHHPG
C112 CLLVTLACHHPGDFT
S125 FTPAMHASLDKFLAs
S132-p SLDKFLAsVStVLTS
S134 DKFLAsVStVLTSkY
T135-p KFLAsVStVLTSkYR
T138 AsVStVLTSkYR___
S139 sVStVLTSkYR____
K140-ac VStVLTSkYR_____
K140 VStVLTSKYR_____
Y141 StVLTSkYR______
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